| Literature DB >> 22505524 |
Rithwik Ramachandran1, Azza Eissa, Koichiro Mihara, Katerina Oikonomopoulou, Mahmoud Saifeddine, Bernard Renaux, Eleftherios Diamandis, Morley D Hollenberg.
Abstract
We compared signalling pathways such as calcium transients, MAPK activation, β-arrestin interactions and receptor internalization triggered by kallikrein-related peptidases (KLKs) 8 and 14 in human and rat proteinase-activated receptor (PAR)2-expressing human embryonic kidney (HEK) and Kirsten transformed rat kidney (KNRK) cells. Further, we analysed processing by KLK8 vs. KLK14 of synthetic human and rat PAR2-derived sequences representing the cleavage-activation domain of PAR2. Our data show that like KLK14, KLK8 can unmask a PAR2 receptor-activating sequence from a peptide precursor. However, whilst KLK8, like KLK14, can signal in rat-PAR2-expressing KNRK cells, this enzyme cannot signal via human PAR2 in HEK or KNRK cells, but rather, disarms HEK PAR1. Thus, KLK8 and KLK14 can signal differentially via the PARs to affect tissue function.Entities:
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Year: 2012 PMID： 22505524 DOI： 10.1515/hsz-2011-0251
Source DB: PubMed Journal: Biol Chem ISSN： 1431-6730 Impact factor: 3.915